› 3ne4

X-ray diffraction
1.81Å resolution

1.8 Angstrom structure of intact native wild-type alpha-1-antitrypsin

Released:
DOI: 10.2210/pdb3ne4/pdb
PDB entry 3ne4 coloured by chain, front view.
PDB entry 3ne4 coloured by chain, side view.
PDB entry 3ne4 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Therapeutic target-site variability in α1-antitrypsin characterized at high resolution.
Patschull AO, Segu L, Nyon MP, Lomas DA, Nobeli I, Barrett TE, Gooptu B
Acta Crystallogr Sect F Struct Biol Cryst Commun 67 1492-7 (2011)
PMID: 22139150

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133784 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Alpha-1-antitrypsin Chain: A
Molecule details ›
Chain: A
Length: 424 amino acids
Theoretical weight: 47.62 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P01009 (Residues: 48-418; Coverage: 94%)
Gene names: AAT, PI, PRO0684, PRO2209, SERPINA1
Sequence domains: Serpin (serine protease inhibitor)
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-1
Spacegroup: C2
Unit cell:
a: 114.38Å b: 38.94Å c: 88.83Å
α: 90° β: 104.29° γ: 90°
R-values:
R R work R free
0.19 0.187 0.233
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Therapeutic targeting of misfolding and conformational change in α1-antitrypsin deficiency.
Nyon et al. (2014)
13 other articles

22 mentions without citation

Engineering the serpin α1 -antitrypsin: A diversity of goals and techniques.
Scott et al. (2020)
21 more